The primary structure of the presumable BChl d-binding polypeptide of Chlorobium vibrioforme f. thiosulfatophilum.
In addition to the previous isolated and sequenced polypeptides from green photosynthetic sulfur bacteria, which are presumably involved in binding BChl c and e, an analogous polypeptide has been purified from the BChl d-containing bacterium Chlorobium vibrioforme f. thiosulfatophilum. The primary structure of this 6.15 kDa polypeptide was determined. It shows an extremely high homology (98.3%) to the corresponding polypeptide from Pelodictyon luteolum, indicative of an important functional role.
Wagner-Huber
R
R
Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.
Fischer
U
U
Brunisholz
R
R
Rümbeli
M
M
Frank
G
G
Zuber
H
H
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D002841:Chromatiaceae / Q000235:genetics / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D045342:Light-Harvesting Protein Complexes; D008969:Molecular Sequence Data; D008970:Molecular Weight; D045322:Photosynthetic Reaction Center Complex Proteins / Q000235:genetics / Q000302:isolation & purification*; D012689:Sequence Homology, Nucleic Acid
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; C067362:BChl-d binding protein, Chlorobium vibrioforme